Donella-Deana A, Monti E, Pinna L A
Dipartimento di Chimica Biologica dell'Universita' di Padova, Italy.
Biochem Biophys Res Commun. 1989 May 15;160(3):1309-15. doi: 10.1016/s0006-291x(89)80146-9.
Adriamycin, a lipid-interacting anti-cancer agent, was found to inhibit the phosphorylation of polyGlu/Tyr (4:1) by tyrosine protein kinases either from spleen or expressed by the oncogene of Abelson murine leukemia virus. The dose dependent inhibition by adriamycin is accounted for by competition for the ATP binding site, but it is also deeply influenced by the nature and concentration of the phosphorylatable substrate, suggesting multiple interactions with the enzyme. The phosphorylation at tyrosine residues of cytosolic proteins from cells transformed by Abelson leukemia virus and the autophosphorylation of tyrosine protein kinases are also inhibited by adriamycin. Unlike tyrosine protein kinases most serine/threonine specific protein kinases, with the notable exception of protein kinase-C, appear to be relatively insensitive to adriamycin.
阿霉素是一种能与脂质相互作用的抗癌药物，它被发现可抑制来自脾脏的酪氨酸蛋白激酶或由阿贝尔森鼠白血病病毒癌基因表达的酪氨酸蛋白激酶对聚谷氨酸/酪氨酸（4:1）的磷酸化作用。阿霉素的剂量依赖性抑制作用是由其对ATP结合位点的竞争所致，但它也深受可磷酸化底物的性质和浓度的影响，这表明它与该酶存在多种相互作用。阿霉素还可抑制由阿贝尔森白血病病毒转化的细胞中胞质蛋白酪氨酸残基的磷酸化以及酪氨酸蛋白激酶的自身磷酸化。与酪氨酸蛋白激酶不同，大多数丝氨酸/苏氨酸特异性蛋白激酶，蛋白激酶-C是显著的例外，似乎对阿霉素相对不敏感。
